MolNFT v1 · #19376 · protein

Specific chemical and structural damage at nine time points (point H) caused by intense synchrotron radiation to torpedo californica acetylcholinesterase

1QIK: “Specific chemical and structural damage at nine time points (point H) caused by intense synchrotron radiation…”. X-ray diffraction, 6 pockets (best druggability 0.78). MolNFT v1 #19376 on GenesisL1: 3D structure, binding sites and…

PDB: 1QIK
Type: protein
Length: 532 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetylcholinesterase
EC: 3.1.1.7
UniProt: P04058
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetylcholinesterase (EC 3.1.1.7)	protein	532	39% helix, 17% strand	P04058

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	387	0.78	0.87	35	empty
2	338	0.57	0.75	32	empty
3	116	0.42	0.76	21	empty
4	60	0.33	0.77	12	empty
5	71	0.31	0.74	17	empty

Compared structures

1QIK · Specific chemical and structural damage at nine time points (point H) caused by intense… · the same entry in another collection · chain A against A, TM-score 1.00
P04058 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P04058) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P04058
Elsewhere: RCSB PDB 1QIK · PDBe 1QIK · UniProt P04058

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